Lilja H, Weiber H
Scand J Clin Lab Invest. 1983 Jun;43(4):307-12.
Most of the gamma-glutamyltransferase occurring in semen was found to be bound to the membranes of prostatic organelles, as is the case with Mg++-Ca++-dependent ATPase, and Zn++-dependent peptidase hydrolysing succinyl (alanine)3-paranitroanilide. Organelle-bound gamma-glutamyltransferase was released in a water-soluble form by papain. Charge shift electrophoresis revealed the presence in seminal fluid of a small additional amount of gamma-glutamyltransferase that is unbound and water-soluble, but also of prostatic origin. After papain treatment there was no sign of the organelle-bound Zn++-dependent peptidase activity, nor of the Mg++-Ca++ dependent ATPase activity, both having been inactivated by the papain. Both organelle-bound gamma-glutamyltransferase and Zn++-dependent peptidase could be rendered soluble in active form with the non-ionic detergent Triton X-100.
研究发现，精液中出现的大多数γ-谷氨酰转移酶都与前列腺细胞器的膜结合，Mg++-Ca++依赖性ATP酶以及水解琥珀酰（丙氨酸）3-对硝基苯胺的Zn++依赖性肽酶也是如此。木瓜蛋白酶可将细胞器结合的γ-谷氨酰转移酶以水溶性形式释放出来。电荷转移电泳显示，精液中还存在少量未结合且水溶性的γ-谷氨酰转移酶，但其也源自前列腺。木瓜蛋白酶处理后，未发现细胞器结合的Zn++依赖性肽酶活性以及Mg++-Ca++依赖性ATP酶活性的迹象，这两种酶均已被木瓜蛋白酶灭活。细胞器结合的γ-谷氨酰转移酶和Zn++依赖性肽酶都可以用非离子去污剂Triton X-100使其以活性形式溶解。
